ID G6PD_ZYMMO Reviewed; 485 AA. AC P21907; Q5NQL3; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 04-NOV-2026, entry version 150. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966}; GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=ZMO0367; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Sphingomonadales; Zymomonadaceae; Zymomonas. OX NCBI_TaxID=264203; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=2254282; DOI=10.1128/jb.172.12.7227-7240.1990; RA Barnell W.O., Yi K.C., Conway T.; RT "Sequence and genetic organization of a Zymomonas mobilis gene cluster that RT encodes several enzymes of glucose metabolism."; RL J. Bacteriol. 172:7227-7240(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RA Ahn J.Y., Kang H.S.; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., RA Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5- CC lactone + NADPH + H(+); Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00966}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00966}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M60615; AAA27692.1; -; Genomic_DNA. DR EMBL; AF313764; AAG29865.1; -; Genomic_DNA. DR EMBL; AE008692; AAV88991.1; -; Genomic_DNA. DR PIR; B37855; B37855. DR RefSeq; WP_011240288.1; NC_006526.2. DR PDB; 7XHL; X-ray; 3.25 A; A/B/C/D/E/F/G/H=1-485. DR PDB; 7XHP; X-ray; 2.78 A; A/B/C/D/E/F/G/H=1-485. DR AlphaFoldDB; P21907; -. DR SMR; P21907; -. DR STRING; 264203.ZMO0367; -. DR GeneID; 79904429; -. DR KEGG; zmo:ZMO0367; -. DR eggNOG; COG0364; Bacteria. DR HOGENOM; CLU_013524_5_0_5; -. DR OMA; AACAMFI; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000001173; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00871; zwf; 1. DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1. DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glucose metabolism; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..485 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068138" FT ACT_SITE 236 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 46 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 89..90 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 144 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 231 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 334 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:7XHL" FT STRAND 12..15 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 18..22 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 24..31 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:7XHL" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:7XHL" FT HELIX 51..61 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:7XHL" FT HELIX 73..77 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:7XHL" FT HELIX 94..99 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:7XHL" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:7XHL" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:7XHL" FT HELIX 121..125 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 150..163 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 174..177 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 184..189 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 199..211 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 220..225 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 229..237 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 238..245 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 254..266 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 273..279 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 287..290 FT /evidence="ECO:0007829|PDB:7XHL" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:7XHL" FT HELIX 298..302 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 310..318 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 320..323 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 327..335 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 341..347 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 354..358 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 366..374 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 376..384 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 395..403 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 404..407 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 416..425 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 430..433 FT /evidence="ECO:0007829|PDB:7XHP" FT HELIX 435..454 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:7XHP" FT STRAND 466..468 FT /evidence="ECO:0007829|PDB:7XHL" FT HELIX 471..477 FT /evidence="ECO:0007829|PDB:7XHP" FT TURN 478..480 FT /evidence="ECO:0007829|PDB:7XHP" SQ SEQUENCE 485 AA; 53859 MW; C326FC605ED92430 CRC64; MTNTVSTMIL FGSTGDLSQR MLLPSLYGLD ADGLLADDLR IVCTSRSEYD TDGFRDFAEK ALDRFVASDR LNDDAKAKFL NKLFYATVDI TDPTQFGKLA DLCGPVEKGI AIYLSTAPSL FEGAIAGLKQ AGLAGPTSRL ALEKPLGQDL ASSDHINDAV LKVFSEKQVY RIDHYLGKET VQNLLTLRFG NALFEPLWNS KGIDHVQISV AETVGLEGRI GYFDGSGSLR DMVQSHILQL VALVAMEPPA HMEANAVRDE KVKVFRALRP INNDTVFTHT VTGQYGAGVS GGKEVAGYID ELGQPSDTET FVAIKAHVDN WRWQGVPFYI RTGKRLPARR SEIVVQFKPV PHSIFSSSGG ILQPNKLRIV LQPDETIQIS MMVKEPGLDR NGAHMREVWL DLSLTDVFKD RKRRIAYERL MLDLIEGDAT LFVRRDEVEA QWVWIDGIRE GWKANSMKPK TYVSGTWGPS TAIALAERDG VTWYD //